DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Status of the Claims
Claims 1-15, 22, and 27-31 are pending; claims 22, 27, and 31 are withdrawn; claims 16-21 and 23-26 are canceled; claims 1-2, 5, 8-10, and 14-15 are amended; Claims 1-15 and 28-30 are examined below.
Priority
The present application was filed 01/26/2021 and claims benefit under 35 U.S.C. 119(e) to national stage entry of PCT/GB2019/052101, which in turn claims foreign priority to GB1812331.5, filed 07/27/2018.
Withdrawn/maintained Rejections
The rejection of claims 1-15 and 28-30 under 35 U.S.C. 112(b) because of the use of the term “preferably” in claims 1-2, 8, 10, and 15, is withdrawn due to the amendment of said claims.
The rejection of claims 1-14 under 35 U.S.C. 103 is withdrawn due to the amendment of the claim.
The rejection of claims 15 and 28-30 under 35 U.S.C. 103 is maintained for the reasons of record and reiterated below.
The rejection of claims 1-15 and 28-30 under 35 U.S.C. 112(a) is maintained, see below.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-15 and 28-30 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim 1 recites “(ii) […] capture molecules capable of binding to the capture site of the indicator molecule”. Claim 15 recites “an antibody specific for the de-sialylated form of the peptide comprising SEQ ID NO: 11, 12, 13, 14, 15, or 16”. The specification on page 12, lines 1-5 recites that the indicator molecule and the capture molecule are two halves of a binding pair selected from a list comprising: an antigen – antibody or binding fragment thereof, biotin and avidin, and immunoglobulin and protein A or G, a carbohydrate and a lectin, complementary nucleotide sequences, a ligand and a receptor molecule and others. The claims encompass a large genus of products that may be characterized by substantial variability. Claim 15 does recite the light and heavy chain sequences of the binding molecule, but only in the alternative to the “antibody specific for the de-sialylated form of the peptide”.
Even limited to the limitation of antibodies, such as “capable of biding to the capture site” (claim 1) and “specific for the de-sialylated form of the peptide” (claim 15), the claims encompass a large and highly variable genus. The claims place no limitation on the sequence/structure of the antibodies themselves, and rather define the antibodies only in terms of desired binding properties.
The claim scope is potentially enormous depending on how many of the products that meet the structural requirement would also meet the functional requirements (i.e., binding the capture site of the indicator molecule or binding the de-sialylated derivative of the indicator molecule). Furthermore, the specification fails to disclose sufficient identifying characteristics of the genus (the claimed antibodies), as discussed in more detail below, such that one having ordinary skill in the art can readily visualize the species encompassed by the claimed genus (i.e., what antibodies meeting the structural requirement also exhibit the required functional, namely binding, requirement).
“[T]he purpose of the written description requirement is to ‘ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description requirement, the specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir. 1991). See also MPEP 2163.04.
For a claim to a genus, a generic statement that defines a genus of substances by only their functional activity does not provide an adequate written description of the genus. Regents of the University of California v. Eli Lilly, 43 USPQ2d 1398 (CAFC 1997). The recitation of a functional property alone, which must be shared by the members of the genus, is merely descriptive of what the members of the genus must be capable of doing, not of the substance and structure of the members. The Federal Circuit has cautioned that, for claims reciting a genus of antibodies with particular functional properties (e.g., high affinity, neutralization activity, competing with a reference antibody for binding, binding to a certain epitope), “[c]laiming antibodies with specific properties, e.g., an antibody that binds to human TNF-α with A2 specificity, can result in a claim that does not meet written description even if the human TNF-α protein is disclosed because antibodies with those properties have not been adequately described." Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1875, 1877-78 (Fed. Cir. 2011).
Along these same lines, a more recent Federal Circuit decision, Amgen v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017), describes how when an antibody is claimed, 35 U.S.C. § 112(a) requires adequate written description of the antibody itself; not just a description of the sequence to which the antibody binds. Amgen, 872 F.3d at 1378-79.
It is true that functionally defined claims can meet the written description requirement if a reasonable structure-function correlation is established, whether by the inventor as described in the specification or known in the art at the time of the filing date” (AbbVie, 759 F.3d at 1298, reiterating Enzo Biochem, Inc., 323 F.3d at 964)(emphasis added).
In the present case, however, there is insufficient evidence of such an established structure-function correlation in the case of antibodies that bind the capture site of the indicator molecule or the de-sialylated derivative of the indicator molecule.
A claimed invention may not be adequately described where an invention is described solely in terms of a method of its making coupled with its function and there is no described or art recognized correlation or relationship between the structure of the invention and its function. A biomolecule defined solely by its ability to perform a function, such as to serve as an antigen recognizing construct, without a known or disclosed correlation between that function and the structure of the sequence, normally is not a sufficient identifying characteristic for written description purposes, even when accompanied by a method of obtaining the biomolecule of interest. See MPEP 2163.
As discussed in the recent case of Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017), see page 17:
An adequate written description must contain enough information about the actual makeup of the claimed products—“a precise definition, such as by structure, formula, chemical name, physical properties, or other properties, of species falling within the genus sufficient to distinguish the genus from other materials,” which may be present in “functional” terminology “when the art has established a correlation between structure and function.” Ariad, 598 F.3d at 1350. But both in this case and in our previous cases, it has been, at the least, hotly disputed that knowledge of the chemical structure of an antigen gives the required kind of structure-identifying information about the corresponding antibodies. See, e.g., J.A. 1241 (549:5–16) (Appellants’ expert Dr. Eck testifying that knowing “that an antibody binds to a particular amino acid on PCSK9 . . . does not tell you anything at all about the structure of the antibody”); J.A. 1314 (836:9–11) (Appellees’ expert Dr. Petsko being informed of Dr. Eck’s testimony and responding that “[m]y opinion is that [he’s] right”); Centocor, 636 F.3d at 1352 (analogizing the antibody- antigen relationship as searching for a key “on a ring with a million keys on it”) (internal citations and quotation marks omitted).
Amgen Inc. v. Sanofi further notes, pointing to Ariad Pharms., Inc. v. Eli Lilly & Co., 94 USPQ2d 1161 (Fed Cir. 2010):
To show invention, a patentee must convey in its disclosure that it “had possession of the claimed subject matter as of the filing date.” Id. at 1350. Demonstrating possession “requires a precise definition” of the invention. Id. To provide this “precise definition” for a claim to a genus, a patentee must disclose “a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Id. Amgen at pages 7-8.
In the present case it is also noted that the claims are not limited to any particular epitope of a specific peptide. For example, the claims are not limited to any particular epitope sequence to which the antibody binds, and rather broadly encompass that the antibodies bind the capture site of the indicator molecule or the de-sialylated derivative of the indicator molecule. Nonetheless, , even if limited to a particular antigen structure, the art recognizes that structure (of a particular antigen) is not necessarily a reliable indicator of function, so even if the claim was reciting a particular antigen sequence to which the antibody binds, there still may be insufficient written description to support the entire genus as claimed.
Recent court cases have indicated that recitation of an antibody which has specific functional properties in the absence of knowledge of the antibody sequences that give rise to said functional properties do not satisfy the requirements for written description. See AbbVie Deutschland GmbH v. Janssen Biotech. Inc. as well as Amgen v. Sanofi, as discussed above. Indeed, in Amgen the court indicates that that it is improper to allow patentees to claim antibodies by describing something that is not the invention, i.e. the antigen, as knowledge of the chemical structure of an antigen does not give the required kind of structure-identifying information about the corresponding antibodies, with the antibody-antigen relationship be analogized as a search for a key on a ring with a million keys on it.
The specification, in disclosing only one species of antibody specific for the de-sialylated form of the peptide, at best describes plans for making additional antibodies/ binding agents and then identifying those that satisfy claim limitations, but a mere “wish or plan” for obtaining the claimed invention is not sufficient. Centocor Ortho Biotech Inc. v. Abbott Laboratories, 97 USPQ2d 1870 (Fed. Cir. 2011).
The teachings of Harlow et al. (Antibodies, A Laboratory Manual, Cold Spring Harbor laboratory, 1988, pages 25-26 and 37-59, cited herewith; PTO-892 06/26/2025) which describe how the steps of the humoral immune response to an immunogen are dependent on APC, T-cell and B-cell recognition and processing of the immunogen in ways well known in the art to be highly unpredictable and heavily influenced by the particular immunogen and the specifics of the immunization protocol. Harlow et al. teach that even small changes in structure, such as loss of a single hydrogen bond, can profoundly affect antibody-antigen interaction (p. 25, last paragraph to page 26, second paragraph).
The principles laid out in Harlow are further illustrated in the teachings of Edwards et al. ("The remarkable flexibility of the human antibody repertoire; isolation of over one thousand different antibodies to a single protein, BLyS" J. Mol. Biol. (2003) 334, 103–118, DOI: 10.1016/j.jmb.2003.09.054; PTO-892 06/26/2025), which shows the immense combinatorial flexibility and capacity of the human antibody repertoire to generate binding sites to an individual protein antigen, the B-lymphocyte growth factor known as “BLyS” (see entire document). Edwards describes in detail how the breadth of antibody structures against a given immunogen can be influenced by the immunization and/or selection methods (see Discussion Section).
As yet another example to illustrate the potential scope of the genus of antibodies encompassed by the instant claims, consider the teachings of Meyer et al. (“New Insights in Type I and II CD20 Antibody Mechanisms-Of-Action With a Panel of Novel CD20 Antibodies”, British Journal of Haematology, 2018, 180, 808–820, |https://doi.org/10.1111/bjh.15132; PTO-892 06/26/2025). Meyer describes the core binding region of the well-known anti-CD20 antibody rituximab corresponds to amino acid residues 170ANPS173, wherein N171 is the key residue for binding. By contrast, the OBZ and B1 anti-CD20 antibodies share an overlapping epitope with rituximab (170ANPSEKNSP178); however, in contrast to rituximab residues at positions 176–178 contribute the most to binding (see page 809, left col., 2nd full paragraph). Meyer also described the production and characterization of a panel of new anti-CD20 antibodies which were shown to bind epitopes contained within or nearby the rituximab 170ANPS173 epitope but to bind to different residues than rituximab binds in this region (see page 811, “New CD20 mAbs with overlapping, but distinct epitopes,” see also page 815-16 bridging paragraph).
More particularly, Meyer teaches the newly created anti-CD20 mAbs m1 and m2 were found to bind within but also in the vicinity of the rituximab binding site (m1 and m2) and elsewhere (m2):
“detailed epitope mapping was performed for both mIgG2c-CD20 mAbs m1 and m2, by using PepScan technology. We identified the critical residues of m1 to be 168EPANPSEK175 by using linear (Figure S2A) and circular (Fig 2C, left) peptides with a positional amino acid scan covering the larger extracellular loop. Also for m2, a signal decrease below the WT binding signal occurred within the 168EPANPSEK175 sequence motif but the binding signal to the linear (Figure S2B) and circular (Fig 2C, right) peptide was rather low. This suggests that the epitope of both mAbs is located on the larger loop in the same region, however their binding characteristics are different. The data suggests that m1 binds a linear epitope, whereas m2 binds to a conformational epitope.” (see ibid). Moreover, while these antibodies bind within or nearby the rituximab 170ANPS173 epitope they do so with heavy and light chain CDRs non-homologous to those of rituximab.
The specification fails to provide adequate written description for the genus of antibodies claimed, as the antibodies are described only in terms of desired function properties and not in terms of common structure or other relevant identifying characteristics to define the genus and there is no apparent structure-function correlation which would allow one to readily visualize what species would and would not be encompassed by the claimed invention. The specification does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 15 and 28-29 are rejected under 35 U.S.C. 103 as being unpatentable over Davis et al. (WO 2015/059487; PTO-892 06/26/2025) in view of Monti et al. Sialidases in vertebrates: a family of enzymes tailored for several cell functions. Advances in carbohydrate chemistry and biochemistry. 2010 Jan 1;64:403-79 (PTO-892 06/26/2025) and Sugawara et al. (JP2013231012A; PTO-892 06/26/2025).
Regarding claim 15, the claim recites parts of a composition in the alternative. The prior art teaches “(d) an indicator molecule suitable […] comprising a capture site and a peptide comprising: X1-X2-X3[Gal-Sial]-X4-X5“.
Davis teaches an enzyme detection kit for detecting the presence of cleavage activity of an enzyme capable of cleaving a substrate comprising an indicator molecule for adding to the test sample, said indicator molecule comprising a cleavage region comprising at least one cleavage site, a capture site, wherein cleavage of the at least one cleavage site produces a novel binding site; capture molecules capable of binding to the capture site of the indicator molecule, a solid support to which the capture molecules can be attached to form a capture zone to receive the test sample, and binding molecules capable of binding to the novel binding site, wherein the binding molecules are incapable of binding to the indicator molecule unless and until cleavage has occurred (Davis, page 6, lines 23- 36). Davis further teaches that the indicator molecule also comprises a capture site which is a discrete region of the indicator molecule which permits immobilization of the indicator molecule, whether cleaved or uncleaved, at a capture zone (Davis, page 8, lines 4-6). Davis further teaches that the devices and methods of the invention aim to permit detection of protease activity at low levels or concentration , because it has been found that using antibodies that bind only to cleavage products, but not the uncleaved indicator molecule enables detection of protease activity at low concentrations in particular in urine samples (Davis, page 2, lines 18-22). Davis further teaches that the indicator molecules of the invention may be cleaved by enzymes such as neuraminidases (sialidase; Davis, page 11, lines 30-33). Davis teaches an indicator molecule comprising a cleavage region comprising at least one cleavage site and further teaches that the indicator molecules of the invention can be cleaved by other enzymes, including neuraminidases (Davis, page 11, lines 30-33). As such Davis teaches a composition comprising an indicator molecule suitable for use in detecting the presence in a test sample of cleavage activity of an enzyme.
Davis fails to teach specifically that the binding molecules can only bind after cleavage of a sialyl group from the indicator molecule. Davis further fails to teach a peptide comprising the sequence X1-X2-X3[Gal-Sial]-X4-X5, where X3 is selected from Ser, Thr, Tur, Hul, Hup, Asn, Arg or SEP and where at least one of the amino acid molecules in position X1, X2, X4, or X5 is a D-amino acid and/or a non-standard amino acid or a non-natural amino acid (claim 15 (d)).
Monti teaches that sialidases or neuraminidase are a family of exo-glycosidases that catalyze the hydrolytic cleavage of non-reducing sialic acid residues linked to the saccharide chains of glycoproteins and glycolipids as well as to oligo- and poly-saccharides. Monti further teaches that they are widely distributed in nature from viruses and microorganisms (such as bacteria, protozoa, and fungi) to vertebrates (Monti, page 405, ‘I. Introduction’, lines 1-6).
Sugawara teaches the following peptide, wherein the peptide comprises 5 amino acids (X1-X2-X3[Gal-Sial]-X4-X5), X3 is Asn. (Sugawara, page 1, ‘Abstract’, ‘Formula 1’):
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Sugawara further teaches that the glycopeptide derivative has sialic acid bonded to galactose at two non-reducing ends (Sugawara, page 6, paragraph [0017], lines 3-4). Sugawara further teaches that the amino acids may be L-amino acid or D-amino acid (Sugawara, page 7, paragraph [0018], lines 5-6). Sugawara further teaches that the glycopeptide derivative is useful because it can immobilize the glycopeptide derivative on a support and the virus species can be determined or the virus can be concentrated (Sugawara, page 13, paragraph [0046], lines 1-6). Sugawara further teaches that hemagglutinin and neuraminidase are present on the surface of influenza virus and that human influenza virus exhibits high affinity for sugar chains having a N-acetylneuraminic acid-α-2,6-galactose and therefore the sialic acid-containing sugar-immobilized particles have a strong affinity for influenza virus and is expected to enable high-sensitivity analysis (Sugawara, page 14, see entire paragraph [0049]). Sugawara further teaches that the glycopeptide derivative is an effective research tool in the field of viral infection diagnosis.
It would have been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified the kit of Davis with binding molecules that can bind the de-sialylated derivative of the indicator molecule, because Davis teaches that the enzyme can be a neuraminidase and that neuraminidases cleave sialic acid residues.
It would have further been prima facie obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified the kit of Davis with the glycopeptide of Sugawara because of the teaching of Sugawara that the glycopeptide has a strong affinity for influenza virus and is expected to enable high-sensitivity analysis. The ordinary artisan would be motivated to do so, because of the teaching of Sugawara that the glycopeptide derivative is an effective research tool in the field of viral infection diagnosis. As such, the limitations of claim 1 and claim 15 are obvious over the combination of the prior art.
The ordinary artisan would have a reasonable expectation of success because both the kit of Davis and the glycopeptide of Sugawara have specificity for neuraminidase/sialidase enzymes.
Regarding claim 28, Davis teaches an enzyme detection device that comprises binding molecules (Davis, page 3, line 4). Davis further teaches that the binding molecules is for example an antibody (Davis, page 11, line 5). Davis teaches that the binding molecule may be directly or indirectly labeled with a reporter molecule (Davis, page 24, line 31).
Regarding claim 29, Davis further teaches that the reporter molecule can be a gold particle (Davis, page 24, lines 35-36).
Allowable Subject Matter
Claims 1 and dependent claims 2-14 appear to be free of the prior art.
Note that independent claim 1 is also rejected under 35 U.S.C. §112(a).
Claim 30 is objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
The following is a statement of reasons for the indication of allowable subject matter:
Claim 1 is free of the prior art because, while Davis teaches a binding molecule that is an antibody, it does not teach sequences of the claimed heavy and light chain CDRs (SEQ ID Nos: 1-6).
Claims 5-6, 8, 13-14, and 30 are free of the prior art because the closest prior art, Davis et al. WO 2015/059487, while it does teach an enzyme detection kit for detecting the activity of an enzyme capable of cleaving a substrate comprising an indicator molecule, does not teach indicator molecules comprising SEQ ID NOs: 10-16.
Claim 9 is free of the prior art because, while Davis teaches a binding molecule that is an antibody, it does not teach sequences of the claimed heavy and light chains (SEQ ID Nos: 7-8).
Response to Arguments
Applicant's arguments filed 09/25/2025 regarding the rejection under 35 U.S.C. §112(a) have been fully considered but they are not persuasive.
Applicant argues on page 12 that claim 1 is amended to incorporate the subject matter of claim 9 defining the binding molecules as antibodies and the antibodies by complementarity determining region and thus the claimed device and kits comply with the written description requirement.
This argument is not persuasive.
While the sequences of SEQ ID NOs: 1-6 (as recited in newly amended claim 1) define the binding molecule capable of binding to the de-sialylated derivative of the indicator molecule (claim 1, iii), the binding molecule “capable of binding to the capture site of the indicator molecule, irrespective of whether or not the indicator molecule has been cleaved” (claim 1, ii) is not described by a sequence. The binding molecule is described by what it binds and not what it is and as such it is maintained that claim 1 fails to comply with the written description requirement.
Claim 15 is not dependent from claim 1 and the “antibody specific for the de-sialylated form of the peptide” of claim 15 (a) has not been amended to comprise the sequences of the complementary determining regions. The limitations of claim 15 (a) and (b) are recited in the alternative and as such the rejection is maintained.
For all the reasons above, the arguments are not persuasive.
Regarding applicant’s remarks, page 12, the rejection under 35 U.S.C. §112(b) has been withdrawn due to the amendment of the claims.
Regarding applicant’s remarks, page 12-13, the rejection of claims 1-14 under 35 U.S.C. §103 has been withdrawn due to the amendment of the claims. However, the rejection of claim 15 and 28-30 is maintained because claim 15 recites a composition comprising “an antibody specific for the de-sialylated form of the peptide […] or (b) an antibody having a […] SEQ ID NO:1; […] or (d) an indicator molecule suitable for use in detecting the presence”. As such, the claim recites the parts of the composition in the alternative and because the art teaches a composition comprising an indicator molecule suitable for use in detecting the presence in a test sample of cleavage activity of a sialidase enzyme comprising X1-X2-X3[Gal-Sial]-X4-X5, the prior art meets the limitation of the claim.
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/STEFANIE J. KIRWIN/Examiner, Art Unit 1677
/BAO-THUY L NGUYEN/Supervisory Patent Examiner, Art Unit 1677 March 2, 2026